Publications by authors named "Federica Basilico"
Article Synopsis
- Chromosomes play a crucial role in carrying genetic material, and kinetochores help ensure their accurate transfer during cell division by connecting them to the mitotic spindle.
- Kinetochores are complex structures made up of various protein subunits, with the inner kinetochore formed by a group of centromeric proteins (CCAN), and the outer kinetochore created by the KMN network, which binds microtubules.
- The study reveals how a specific CCAN subcomplex (CHIKMLN) increases the binding selectivity for CENP-A nucleosomes, forming a strong link between CENP-A and microtubules, and sheds light on the organization and function of kinetocho
Article Synopsis
- Kinetochores are essential protein complexes that form on centromeres, binding to spindle microtubules to ensure proper chromosome separation during cell division.
- The study focuses on CENP-C, a key component of the constitutive centromere-associated network (CCAN), which facilitates the assembly of kinetochores and connects centromeres with microtubules.
- The researchers discovered that the PEST domain in CENP-C directly interacts with the CENP-HIKM subcomplex, revealing how CENP-C helps target other CCAN subunits to the kinetochore, highlighting its role in the overall assembly process.
We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
View Article and Find Full Text PDFKinetochores, multi-subunit complexes that assemble at the interface with centromeres, bind spindle microtubules to ensure faithful delivery of chromosomes during cell division. The configuration and function of the kinetochore-centromere interface is poorly understood. We report that a protein at this interface, CENP-M, is structurally and evolutionarily related to small GTPases but is incapable of GTP-binding and conformational switching.
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